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dc.contributor.authorYu, Xing
dc.contributor.authorDang, Vi T
dc.contributor.authorFleming, Fiona E
dc.contributor.authorvon Itzstein, Mark
dc.contributor.authorCoulson, Barbara S
dc.contributor.authorBlanchard, Helen
dc.date.accessioned2018-01-23T01:01:21Z
dc.date.available2018-01-23T01:01:21Z
dc.date.issued2012
dc.date.modified2013-06-17T02:42:07Z
dc.identifier.issn0022-538X
dc.identifier.doi10.1128/JVI.06975-11
dc.identifier.urihttp://hdl.handle.net/10072/48644
dc.description.abstractThe rotavirus spike protein domain VP8* is essential for recognition of cell-surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-acetylneuraminic acids occur naturally in both animals and humans whereas N-glycolylneuraminic acids are present only through dietary uptake in normal human tissues. The preference of animal rotaviruses towards these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* towards N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from porcine rotavirus CRW-8 and bovine rotavirus NCDV showed preference for N-glycolyl- over N-acetylneuraminic acids, contrasting with monkey rotavirus RRV. Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl- or N-glycolyl-moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157 to Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_US
dc.publisherAmerican Society for Microbiology
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom13456
dc.relation.ispartofpageto13466
dc.relation.ispartofissue24
dc.relation.ispartofjournalJournal of Virology
dc.relation.ispartofvolume86
dc.rights.retentionY
dc.subject.fieldofresearchBiomolecular Modelling and Design
dc.subject.fieldofresearchProteins and Peptides
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchAgricultural and Veterinary Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode030402
dc.subject.fieldofresearchcode030406
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode07
dc.subject.fieldofresearchcode11
dc.titleStructural Basis of Rotavirus Strain Preference toward N-Acetyl- or N-Glycolylneuraminic Acid-Containing Receptors
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomics
gro.date.issued2012
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark
gro.griffith.authorCoulson, Barbara
gro.griffith.authorBlanchard, Helen
gro.griffith.authorYu, Xing


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